The cecropins are a group of potent antimicrobial peptides, initially discovered in insects but later found in other animals including mammals. Synthetic peptide chemistry has played an important role in establishing their primary sequences, as well as the steps in the processing of the biosynthetic preprocecropins. Solid-phase peptide synthesis has been the method of choice. Synthetic chimeric peptides have led to more active products and a better understanding of their mode of action. The structural requirements for high activity include a basic amphipathic N-terminus, a short central flexible sequence and a hydrophobic helical C-terminus. Cecropin-melittin hybrids as small as 15 residues are highly active. In planar lipid bilayers the cecropins form pores which pass ions and carry a current under a voltage gradient. Synthetic D-enantiomers of several antibacterial peptides carry the same current as the natural all-L-peptides and are equally active against several test bacteria. Therefore, the activity is not dependent on chiral interactions between the peptides and the lipid bilayers or the bacterial membranes. Recent examination of retro and retroenantio peptides has further defined the limits of the structural requirements of these peptides. Some of the hybrid peptides are active against Plasmodium falciparum and Mycobacterium smegmatis.